ID A0A1S3HEM0_LINUN Unreviewed; 667 AA.
AC A0A1S3HEM0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Dual specificity protein phosphatase 16 isoform X2 {ECO:0000313|RefSeq:XP_013383484.1};
GN Name=LOC106153898 {ECO:0000313|RefSeq:XP_013383484.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013383484.1};
RN [1] {ECO:0000313|RefSeq:XP_013383484.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013383484.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily.
CC {ECO:0000256|ARBA:ARBA00008601}.
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DR RefSeq; XP_013383484.1; XM_013528030.1.
DR AlphaFoldDB; A0A1S3HEM0; -.
DR EnsemblMetazoa; XM_013528030.1; XP_013383484.1; LOC106153898.
DR GeneID; 106153898; -.
DR OrthoDB; 2901840at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd14568; DSP_MKP_classIII; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR008343; MKP.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR10159; DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR10159:SF540; TYROSINE-PROTEIN PHOSPHATASE VHP-1; 1.
DR Pfam; PF00782; DSPc; 1.
DR PRINTS; PR01764; MAPKPHPHTASE.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678}.
FT DOMAIN 44..186
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 107..167
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 198..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 667 AA; 72216 MW; AD3DE41752B9AD3F CRC64;
MGGGFLEFQA TFPALCESKS VDHKGIHASL TSMSQPCLPV SNVGPTRILP FLYLGSQNDA
LSQETMQKNG INYVLNVSLN CPKPPFIQEG HFIRIPVNDN YSAKLLPHFH KAFQYLDKVR
EANGCVLVHC LAGISRSPTL AIAYIMQHYS MTSEEAYRYV KDKRPTISPN FNFLGQLLEY
EKQMKRYCSP LVTPLPFPPT ATPTPTNQDS PLSWPNPKTS PFSTIQESSS LNAQSPTTAL
AKLNFDQPLT PEAAPSKSSE TSVSPFFPPT RTQLPSPKIP AFKSATLPAS IGCSLRERLS
LTRVQKRSSS PASTSFGSKT ADDLSIGHVP SSDMISSFPT TSLDQLNFTP CFALDESKSK
TSGIKRPHST NTGISQLQTV ESKSESGSVT GKRSWGVGMT ESTTPKESVS HASGTDRTTI
AANPSRSNSN NTSPGLKTTG TKRPLDFGKP LESTHVSGTK SPTAPSPMSP SLINTGDSQV
KLRSPENRAK RQLVRPNSIA FSTYPSFDLG CNGSDSSTSN SPDTKAPKSS NMDMETCKKK
LLLESKKYTN GASTMQTFAS NVALETVLGK SRLFEHCRKS RSLDDILSSP EDERKHASCG
CIKKKMSKSS LLKSAMVADL FPQTMGLEHV QCRCRGASDP HHQSNSSISS SSSHNSLHGS
VEIIQVS
//
